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Database: UniProt
Entry: W9VSB0_9EURO
LinkDB: W9VSB0_9EURO
Original site: W9VSB0_9EURO 
ID   W9VSB0_9EURO            Unreviewed;       451 AA.
AC   W9VSB0;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE            EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN   ORFNames=A1O7_08796 {ECO:0000313|EMBL:EXJ55865.1};
OS   Cladophialophora yegresii CBS 114405.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=1182544 {ECO:0000313|EMBL:EXJ55865.1, ECO:0000313|Proteomes:UP000019473};
RN   [1] {ECO:0000313|EMBL:EXJ55865.1, ECO:0000313|Proteomes:UP000019473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 114405 {ECO:0000313|EMBL:EXJ55865.1,
RC   ECO:0000313|Proteomes:UP000019473};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Cladophialophora yegresii CBS 114405.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC         Evidence={ECO:0000256|RuleBase:RU004273};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC       {ECO:0000256|RuleBase:RU004273}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXJ55865.1}.
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DR   EMBL; AMGW01000006; EXJ55865.1; -; Genomic_DNA.
DR   RefSeq; XP_007760975.1; XM_007762785.1.
DR   AlphaFoldDB; W9VSB0; -.
DR   STRING; 1182544.W9VSB0; -.
DR   GeneID; 19183360; -.
DR   VEuPathDB; FungiDB:A1O7_08796; -.
DR   eggNOG; KOG0372; Eukaryota.
DR   HOGENOM; CLU_004962_8_1_1; -.
DR   OrthoDB; 19833at2759; -.
DR   Proteomes; UP000019473; Unassembled WGS sequence.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd07415; MPP_PP2A_PP4_PP6; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR047129; PPA2-like.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR45619; SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A-RELATED; 1.
DR   PANTHER; PTHR45619:SF8; SERINE_THREONINE-PROTEIN PHOSPHATASE 4 CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00149; Metallophos; 2.
DR   PIRSF; PIRSF033096; PPPtase_5; 2.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU004273};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019473}.
FT   DOMAIN          108..113
FT                   /note="Serine/threonine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS00125"
FT   REGION          162..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          211..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          394..413
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        162..182
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        212..227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   451 AA;  49375 MW;  B9585DB5E280085A CRC64;
     MSDLDKAIAQ LRACRPIPEP QVRELCYKAR ELLIEEGNVV TVDAPVTICG DIHGQFHDLM
     ELFRVGGDVP DTNYLFMGDF VDRGFYSLES FLLLLCLKVR YPDRITLIRG NHESRQITTV
     YGFYDECIRK YGSANVWRYC CEVFDYLALG ALILGATTDV PPSTGSSQGN ESNNNTQSTL
     PPEDEEIESE VLNANGEVVS KSLRRRFEGL SLASEPSQQQ ASNASRISPA PDMDPLEPPT
     SSISSQQSLS GASRSLFTPP TSSTGAVLCV HGGLSPLIET VDKIRLIDRK QEVPHEGAMC
     DLLWSDPDEI EGWGLSPRGA GFLFGADIVR HFNHNNDLSL IARAHQLVME GYKEMFDKTI
     VTVWSAPNYC YRCGNVAAIL ELGEDGSNGG CIQRANGDQG RREPVGGDGN GGGSGVLWNL
     ATPGRRYRVF EAAPQGTRGM PAKKPVGEYF L
//
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